Laboratory of Metabolism, Center for Cancer Research, National Cancer Institute, National Institutes of Health, 9000 Rockville Pike, Bldg. 37, Rm. 3118, Bethesda, MD, 20892-4258, USA.
Cell Mol Life Sci. 2010 Jun;67(12):1957-70. doi: 10.1007/s00018-010-0279-9. Epub 2010 Feb 11.
Members of the polo subfamily of protein kinases have emerged as important regulators in diverse aspects of the cell cycle and cell proliferation. A large body of evidence suggests that a highly conserved polo-box domain (PBD) present in the C-terminal non-catalytic region of polo kinases plays a pivotal role in the function of these enzymes. Recent advances in our comprehension of the mechanisms underlying mammalian polo-like kinase 1 (Plk1)-dependent protein-protein interactions revealed that the PBD serves as an essential molecular mediator that brings the kinase domain of Plk1 into proximity with its substrates, mainly through phospho-dependent interactions with its target proteins. In this review, current understanding of the structure and functions of PBD, mode of PBD-dependent interactions and substrate phosphorylation, and other phospho-independent functions of PBD are discussed.
蛋白激酶的 polo 亚家族成员已成为细胞周期和细胞增殖各个方面的重要调节因子。大量证据表明，polo 激酶 C 端非催化区存在高度保守的 polo 盒结构域 (PBD)，在这些酶的功能中起着关键作用。最近我们对哺乳动物 polo 样激酶 1 (Plk1) 依赖性蛋白-蛋白相互作用机制的理解取得了进展，揭示了 PBD 作为一种重要的分子介体，将 Plk1 的激酶结构域与底物拉近，主要通过与靶蛋白的磷酸化依赖相互作用来实现。在这篇综述中，讨论了 PBD 的结构和功能、PBD 依赖性相互作用和底物磷酸化的模式以及 PBD 的其他非磷酸化依赖功能的当前理解。
